FGF-2 Polyclonal Antibody
¥680.00
MYPT1 (Phospho Ser507) rabbit pAb
活动价：
¥680.00
市场价：¥880.00
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产品规格：
- 50μL
- 100μL
货号：
FAB2612173
- 产品信息
商品描述
靶点-Target
MYPT1
反应性
Human,Mouse,Rat
应用
WB,IHC
宿主物种-Host Species
Rabbit
同种型-Isotype
IgG
修饰-Modification
Phospho
MW(Observed)
130kD
推荐稀释比
WB 1:500-2000;IHC 1:50-300
组成
Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
纯化工艺
The antibody was affinity-purified from rabbit serum by affinity-chromatography using specific immunogen.
储存
-15°C to -25°C/1 year(Do not lower than -25°C)
浓度
1 mg/ml
克隆性
Polyclonal
免疫原
Synthesized phosho peptide around human MYPT1 (Ser507)
特异性
This antibody detects endogenous levels of Human Mouse Rat MYPT1 (phospho-Ser507)
基因名称
PPP1R12A MBS MYPT1
蛋白名称
MYPT1 (Ser507)
别名
Protein phosphatase 1 regulatory subunit 12A;Myosin phosphatase-targeting subunit 1;Myosin phosphatase target subunit 1;Protein phosphatase myosin-binding subunit;
Organism-1
Human
基因ID-1
4659
SwissProt-1
O14974
Organism-2
Mouse
基因ID-2
17931
SwissProt-2
Q9DBR7
Organism-3
Rat
基因ID-3
116670
SwissProt-3
Q10728
背景
Myosin phosphatase target subunit 1, which is also called the myosin-binding subunit of myosin phosphatase, is one of the subunits of myosin phosphatase. Myosin phosphatase regulates the interaction of actin and myosin downstream of the guanosine triphosphatase Rho. The small guanosine triphosphatase Rho is implicated in myosin light chain (MLC) phosphorylation, which results in contraction of smooth muscle and interaction of actin and myosin in nonmuscle cells. The guanosine triphosphate (GTP)-bound, active form of RhoA (GTP.RhoA) specifically interacted with the myosin-binding subunit (MBS) of myosin phosphatase, which regulates the extent of phosphorylation of MLC. Rho-associated kinase (Rho-kinase), which is activated by GTP. RhoA, phosphorylated MBS and consequently inactivated myosin phosphatase. Overexpression of RhoA or activated RhoA in NIH 3T3 cells increased phosph
细胞定位
Cytoplasm . Cytoplasm, cytoskeleton, stress fiber . Also along actomyosin filaments. .
